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The Plant Cell, ISSN 1040-4651, 11/2012, Volume 24, Issue 11, pp. 4465 - 4482
Supramolecular organization of enzymes is proposed to orchestrate metabolic complexity and help channel intermediates in different pathways. Phenylpropanoid... 
Proteins | Enzymes | Lignin | Protein metabolism | Sterols | RESEARCH ARTICLES | Hematocrit | Fluorescence | Cytochromes | Plants | Plant cells | ENDOPLASMIC-RETICULUM MEMBRANE | MOLECULAR-INTERACTIONS | ARABIDOPSIS-THALIANA | BIOCHEMISTRY & MOLECULAR BIOLOGY | CINNAMIC ACID | PHENYLALANINE AMMONIA-LYASE | CYTOCHROME P450 REDUCTASE | PLANT SCIENCES | CELL BIOLOGY | PHENYLPROPANOID PATHWAY | TANDEM AFFINITY PURIFICATION | ENZYME COMPLEXES | BINDING PROTEIN-1 | Green Fluorescent Proteins | Protein Multimerization | Cytochrome P-450 Enzyme System - metabolism | Endoplasmic Reticulum - metabolism | Trans-Cinnamate 4-Monooxygenase - genetics | Acyltransferases - metabolism | Recombinant Fusion Proteins | Coenzyme A Ligases - metabolism | Arabidopsis Proteins - metabolism | Trans-Cinnamate 4-Monooxygenase - metabolism | Lignin - metabolism | Plants, Genetically Modified | Membrane Proteins - metabolism | Transgenes | Acyl Coenzyme A - metabolism | Arabidopsis Proteins - genetics | Hydroxylation | Hydroxybenzoates - metabolism | Membrane Proteins - genetics | Tobacco - metabolism | Arabidopsis - metabolism | Protein Interaction Mapping | Arabidopsis - genetics | Plant Leaves - genetics | Plant Leaves - metabolism | Tobacco - genetics | Cytochrome P-450 Enzyme System - genetics | Phytochemistry | Physiological aspects | Biosynthesis | Research | Protein-protein interactions | Membrane proteins | Index Medicus | Life Sciences | Molecular biology | Cellular Biology | Biochemistry, Molecular Biology
Journal Article
Science, ISSN 0036-8075, 11/2015, Volume 350, Issue 6261, pp. 678 - 680
Journal Article
Molecular Cell, ISSN 1097-2765, 11/2009, Volume 36, Issue 3, pp. 487 - 499
While activation of BAX/BAK by BH3-only molecules (BH3s) is essential for mitochondrial apoptosis, the underlying mechanisms remain unsettled. Here we... 
CELLCYCLE | CYTOCHROME-C | PROAPOPTOTIC BAX | OLIGOMERIZES BAK | BIOCHEMISTRY & MOLECULAR BIOLOGY | ENDOPLASMIC-RETICULUM | SUBCELLULAR LOCATION | PROTEINS | BCL-2 FAMILY-MEMBERS | BH3 DOMAIN | CELL-DEATH | MEMBRANE PERMEABILIZATION | CELL BIOLOGY | bcl-2-Associated X Protein - chemistry | Immunoprecipitation | Apoptosis - drug effects | Protein Multimerization | bcl-2 Homologous Antagonist-Killer Protein - genetics | Immunoblotting | BH3 Interacting Domain Death Agonist Protein - genetics | Green Fluorescent Proteins - genetics | bcl-2 Homologous Antagonist-Killer Protein - metabolism | Bcl-2-Like Protein 11 | Protein Binding - drug effects | Tumor Suppressor Proteins - genetics | Apoptosis Regulatory Proteins - genetics | Membrane Proteins - metabolism | BH3 Interacting Domain Death Agonist Protein - metabolism | bcl-2-Associated X Protein - genetics | Fibroblasts - metabolism | Proto-Oncogene Proteins - metabolism | Green Fluorescent Proteins - metabolism | Tumor Suppressor Proteins - metabolism | Membrane Proteins - genetics | Cells, Cultured | bcl-2-Associated X Protein - metabolism | Etoposide - pharmacology | Proto-Oncogene Proteins - genetics | Mitochondria - metabolism | Apoptosis Regulatory Proteins - metabolism | Mice, Knockout | Animals | Models, Biological | Tunicamycin - pharmacology | Fibroblasts - drug effects | Thapsigargin - pharmacology | Fibroblasts - cytology | Mice | Mutation | Microscopy, Fluorescence | Staurosporine - pharmacology | bcl-2 Homologous Antagonist-Killer Protein - chemistry | Monomers | Apoptosis | Oligomers | Index Medicus
Journal Article
Neuron, ISSN 0896-6273, 09/2013, Volume 79, Issue 6, pp. 1169 - 1182
The gene is located in a chromosomal region linked to various neurological disorders, including intellectual disability, autism, and schizophrenia. CYFIP1... 
MAMMALIAN TARGET | LOCAL PROTEIN-SYNTHESIS | AUTISM | FMRP | MOUSE MODEL | FRAGILE-X-SYNDROME | MECHANISMS | RAC1 | SYNAPTIC PLASTICITY | NEUROSCIENCES | CRITICAL REGION | Humans | Male | Fragile X Mental Retardation Protein - metabolism | Green Fluorescent Proteins - genetics | RNA, Messenger - metabolism | Mental Disorders - genetics | Brain-Derived Neurotrophic Factor - pharmacology | Neurons - ultrastructure | Time Factors | Chromatography, Liquid | Nerve Tissue Proteins - ultrastructure | Enzyme Inhibitors - pharmacology | Mice, Transgenic | Pyrimidines - pharmacology | Synaptosomes - ultrastructure | Analysis of Variance | Indole Alkaloids - pharmacology | Protein Biosynthesis - drug effects | Mice | Carbazoles - pharmacology | Adaptor Proteins, Signal Transducing - chemistry | Synaptosomes - drug effects | Meta-Analysis as Topic | Immunoprecipitation | Age Factors | Synaptosomes - metabolism | Cerebral Cortex - cytology | Microscopy, Immunoelectron | DNA-Binding Proteins - metabolism | Tandem Mass Spectrometry | Nerve Tissue Proteins - chemistry | Transfection | Dendritic Spines - drug effects | Protein Biosynthesis - genetics | Neurons - drug effects | Aminoquinolines - pharmacology | Green Fluorescent Proteins - metabolism | Gene Expression Regulation - genetics | Mice, Inbred C57BL | Cells, Cultured | Nerve Tissue Proteins - genetics | Nerve Tissue Proteins - metabolism | Transcription Factors - metabolism | Animals | Adaptor Proteins, Signal Transducing - genetics | Fragile X Mental Retardation Protein - ultrastructure | Dendritic Spines - genetics | Fragile X Mental Retardation Protein - genetics | Adaptor Proteins, Signal Transducing - metabolism | In Vitro Techniques | Dendritic Spines - ultrastructure | Luminescent Proteins - metabolism | Nervous system diseases | Neurosciences | Neurons | Oncology, Experimental | Genes | Polymerization | Schizophrenia | Protein biosynthesis | Research | Genetic translation | Messenger RNA | Actin | Cancer | Proteins | Brain-derived neurotrophic factor | Protein synthesis | Crystal structure | Index Medicus
Journal Article
Science, ISSN 0036-8075, 11/2012, Volume 338, Issue 6108, pp. 810 - 814
Fluorescent proteins (FPs) are widely used as optical sensors, whereas other light-absorbing domains have been used for optical control of protein localization... 
Proteins | Enzymes | Delta cells | NIH 3T3 cells | REPORTS | Fluorescence | Pseudopodia | Dimers | Cell membranes | Optical control | P branes | SPATIOTEMPORAL CONTROL | ACTIVATION | GTPASES | MULTIDISCIPLINARY SCIENCES | LIGHT | INDUCTION | EXCHANGE FACTORS | LOV DOMAIN | LIVING CELLS | MOTILITY | Darkness | NIH 3T3 Cells | Pseudopodia - ultrastructure | Native Polyacrylamide Gel Electrophoresis | Humans | Protein Multimerization | Adaptor Proteins, Vesicular Transport - genetics | Optogenetics | Adaptor Proteins, Vesicular Transport - metabolism | Recombinant Fusion Proteins - metabolism | Viral Nonstructural Proteins - chemistry | Light | Protein Engineering | Serine Endopeptidases - genetics | Luminescent Proteins - chemistry | Adaptor Proteins, Vesicular Transport - chemistry | Cell Membrane - metabolism | Protein Structure, Tertiary | Models, Molecular | Viral Nonstructural Proteins - genetics | Serine Endopeptidases - chemistry | Recombinant Fusion Proteins - chemistry | Animals | Pseudopodia - metabolism | Recombinant Fusion Proteins - genetics | Luminescent Proteins - genetics | Protein Conformation | Viral Nonstructural Proteins - metabolism | Mice | Serine Endopeptidases - metabolism | HeLa Cells | Luminescent Proteins - metabolism | Physiological aspects | Photoreception | Research | Fluorescent proteins | Sensors | Cellular biology | Index Medicus | Activated | Exposure | Optical sensors | Detection
Journal Article
Molecular Cell, ISSN 1097-2765, 09/2016, Volume 63, Issue 6, pp. 951 - 964
Huntington’s disease is one of several neurodegenerative disorders characterized by the aggregation of polyglutamine (polyQ)-expanded mutant protein. How polyQ... 
POLYGLUTAMINE | PROTEIN | FUS | BIOCHEMISTRY & MOLECULAR BIOLOGY | MUTANT HUNTINGTIN | PHASE-TRANSITION | DISEASE | MUTATIONS | INCLUSION-BODY FORMATION | AGGREGATION | PROTEOSTASIS | CELL BIOLOGY | Protein Aggregates | Neurons - pathology | Humans | Protein Multimerization | Peptides - genetics | Green Fluorescent Proteins - genetics | Recombinant Fusion Proteins - metabolism | Ribosomal Proteins - metabolism | Peptides - metabolism | Neurons - metabolism | Gene Ontology | Green Fluorescent Proteins - metabolism | Gene Expression | HSP40 Heat-Shock Proteins - metabolism | HSP40 Heat-Shock Proteins - genetics | Peptides - chemistry | Ribosomal Proteins - genetics | Huntingtin Protein - metabolism | Molecular Sequence Annotation | Bacterial Proteins - genetics | Solubility | Spectrometry, Fluorescence | Single Molecule Imaging - methods | Protein Interaction Mapping | Animals | Cell Line, Tumor | Recombinant Fusion Proteins - genetics | Bacterial Proteins - metabolism | Luminescent Proteins - genetics | Mice | HeLa Cells | Huntingtin Protein - genetics | Mutation | Luminescent Proteins - metabolism | Ubiquitin | Fluorescence spectroscopy | Nervous system diseases | RNA | Heat shock proteins | Fluorescence | Biosynthesis | Genetic transcription | Oligomers | Analysis | Cellular signal transduction | Research institutes | Binding proteins | Protein binding | Index Medicus
Journal Article
Neuron, ISSN 0896-6273, 08/2012, Volume 75, Issue 4, pp. 618 - 632
Mitochondrial abnormalities have been documented in Alzheimer’s disease and related neurodegenerative disorders, but the causal relationship between... 
ALZHEIMERS-DISEASE BRAIN | DOMINANT OPTIC ATROPHY | MITOCHONDRIAL-FUNCTION | MOUSE MODEL | LIGHT-CHAIN | FRONTOTEMPORAL DEMENTIA | AXONAL-TRANSPORT | NEUROSCIENCES | DYNAMIN-RELATED PROTEIN | PHOSPHORYLATION SITES | TRANSGENIC MICE | Neurons - pathology | Microtubule-Associated Proteins - genetics | Tauopathies - genetics | Cytoskeletal Proteins - genetics | Gelsolin - metabolism | Microtubule-Associated Proteins - metabolism | Humans | Actins - metabolism | Tauopathies - pathology | Cytoplasm - metabolism | MicroRNAs - metabolism | Green Fluorescent Proteins - genetics | Mitochondrial Proteins - genetics | Drosophila Proteins - metabolism | GTP-Binding Proteins - genetics | Nerve Degeneration - metabolism | Neurons - ultrastructure | tau Proteins - genetics | Cell Death - genetics | Mitochondria - genetics | Mitochondrial Proteins - metabolism | ATP Synthetase Complexes - metabolism | Cell Cycle Proteins - genetics | Tauopathies - complications | Cytoskeletal Proteins - metabolism | Myosins - metabolism | Cytoplasm - genetics | RNA Interference - physiology | Disease Models, Animal | In Situ Nick-End Labeling | Green Fluorescent Proteins - metabolism | Animals, Genetically Modified | Gene Expression Regulation - genetics | Drosophila | Cell Cycle Proteins - metabolism | Mitochondria - metabolism | Mitochondria - pathology | Mutation - genetics | Animals | GTP Phosphohydrolases - metabolism | Analysis of Variance | GTP Phosphohydrolases - genetics | Gelsolin - genetics | Mice | Drosophila Proteins - genetics | Nerve Degeneration - etiology | Voltage-Dependent Anion Channels - metabolism | GTP-Binding Proteins - metabolism | Nervous system diseases | Actin | Neurons | Utrophin | Myosin | Mitochondrial DNA | Alzheimer's disease | Proteins | Phosphorylation | Mitochondria | Neurotoxicity | Insects | Microscopy | Neurodegeneration | Pathogenesis | Morphology | Mutation | Defects | Index Medicus | Neurodegenerative diseases | Tau protein | Cell death | Elongation
Journal Article
Nature Communications, ISSN 2041-1723, 2014, Volume 5, Issue 1, pp. 5341 - 5341
During bacterial cell division, filaments of the tubulin-like protein FtsZ assemble at midcell to form the cytokinetic Z-ring. Its positioning is regulated by... 
TOPOLOGICAL SPECIFICITY FACTOR | POLAR LOCALIZATION | RAPID POLE | IN-VITRO | CRYSTAL-STRUCTURE | MEMBRANE | MULTIDISCIPLINARY SCIENCES | ESCHERICHIA-COLI | INHIBITOR MINC | BACTERIAL CHROMOSOME SEGREGATION | Z-RING FORMATION | Cytoskeletal Proteins - genetics | Bacterial Proteins - chemistry | Crystallography, X-Ray | Green Fluorescent Proteins - genetics | Recombinant Fusion Proteins - metabolism | Cell Cycle Proteins - chemistry | Cell Membrane - chemistry | Cell Division | Escherichia coli - metabolism | Cell Cycle Proteins - genetics | Cytoskeletal Proteins - metabolism | Cell Membrane - metabolism | Membrane Proteins - metabolism | Binding Sites | Cytoskeleton - chemistry | Genes, Reporter | Green Fluorescent Proteins - metabolism | Gene Expression | Membrane Proteins - genetics | Bacterial Proteins - genetics | Cell Cycle Proteins - metabolism | Adenosine Triphosphatases - metabolism | Models, Molecular | Polymerization | Escherichia coli Proteins - metabolism | Cell Membrane - ultrastructure | Cytoskeletal Proteins - chemistry | Cytoskeleton - ultrastructure | Recombinant Fusion Proteins - chemistry | Escherichia coli - chemistry | Microscopy, Electron | Protein Transport | Liposomes - chemistry | Membrane Proteins - chemistry | Cytoskeleton - metabolism | Escherichia coli Proteins - genetics | Protein Binding | Recombinant Fusion Proteins - genetics | Adenosine Triphosphatases - chemistry | Bacterial Proteins - metabolism | Adenosine Triphosphatases - genetics | Mutation | Escherichia coli Proteins - chemistry | Liposomes - ultrastructure | Escherichia coli - ultrastructure | Index Medicus
Journal Article